ID M5ED57_9FIRM Unreviewed; 491 AA.
AC M5ED57;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CCU78815.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:CCU78815.1};
GN ORFNames=HSACCH_00921 {ECO:0000313|EMBL:CCU78815.1};
OS Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU78815.1, ECO:0000313|Proteomes:UP000012063};
RN [1] {ECO:0000313|Proteomes:UP000012063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL Genome Announc. 1:217-225(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU78815.1}.
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DR EMBL; CAUI01000010; CCU78815.1; -; Genomic_DNA.
DR RefSeq; WP_005488223.1; NZ_CAUI01000010.1.
DR AlphaFoldDB; M5ED57; -.
DR STRING; 1293054.HSACCH_00921; -.
DR eggNOG; COG0579; Bacteria.
DR InParanoid; M5ED57; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000012063; Unassembled WGS sequence.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1.
DR PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CCU78815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012063}.
FT DOMAIN 7..357
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 403..456
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 491 AA; 53534 MW; 4210BE3838A61C8F CRC64;
MSKDKYDVII VGAGVSGCAV AWKLARYNLD ILILEKAPDV ATGTTKANTA IIHAGYNADP
EKQKGRLNKK GNVQIKDIVE DLSVPFEQIG SLVVGMEDDD LSVIDELLEK GKENGVEGLE
IVDKEWLQKE EPHLSDKAVR ALWAPTAGII TPWEFALALA ENAVANGAEI MLETEVQDVY
TEDGKVTGVK TNQGDFAADY VINAAGLYAD DVARMVGIEK IDIHPRKGEY YIYDHAKDFE
INHVLFPIPT KISKGIVCTK TVEDNLLIGP TSDFVDSKED LATTREGLDH VFNGAKKMFP
DLTLKDSIRV FAGLRAADTT EDFVIEAAED VAGFVNVAGI QSPGLSSAPA VADLVAEILE
NEGLTLEEKE DIIETREEPA RFYEISNEER AAYAEEDKEY GQIICRCETV SLKEIKDAIN
GPIPARTVNA VKRRTRAGAG RCQGGFCGPR VTQIIADELG IDTTEVRLEK DNSKIVEHKI
KGLLGSQGDA E
//
